CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.880 | Class I glutamine amidotransferase (GATase) domain |
Domain Context
CATH Clusters
| Superfamily | 3.40.50.880 |
| Functional Family | Protein/nucleic acid deglycase HchA |
Enzyme Information
| 4.2.1.130 |
D-lactate dehydratase.
based on mapping to UniProt P31658
(R)-lactate = methylglyoxal + H(2)O.
-!- The enzyme, described from the fungi Candida albicans and Schizosaccharomyces pombe, converts 2-oxopropanal to (R)-lactate in a single glutathione (GSH)-independent step. -!- The other known route for this conversion is the two-step GSH- dependent pathway catalyzed by EC 4.4.1.5 and EC 3.1.2.6.
|
| 3.1.2.- |
Thiolester hydrolases.
based on mapping to UniProt P31658
|
| 3.5.1.- |
In linear amides.
based on mapping to UniProt P31658
|
| 3.5.1.124 |
Protein deglycase.
based on mapping to UniProt P31658
(1) An N(omega)-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H(2)O = a [protein]-L-arginine + lactate. (2) An N(6)-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H(2)O = a [protein]-L-lysine + lactate. (3) An S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H(2)O = a [protein]-L-cysteine + lactate.
-!- The enzyme, previously thought to be a glyoxalase, acts on glycated L-arginine, L-lysine, and L-cysteine residues within proteins that have been attacked and modified by glyoxal or 2-oxopropanal. -!- The attack forms hemithioacetal in the case of cysteines and aminocarbinols in the case of arginines and lysines. -!- The enzyme repairs the amino acids, releasing glycolate or lactate (70-80% (S)-lactate and 20-30% (R)-lactate), depending on whether the attacking agent was glyoxal or 2-oxopropanal, respectively.
|
UniProtKB Entries (1)
| P31658 |
HCHA_ECOLI
Escherichia coli K-12
Protein/nucleic acid deglycase 1
|
PDB Structure
| PDB | 1PV2 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
A new native EcHsp31 structure suggests a key role of structural flexibility for chaperone function.
Protein Sci.
|